ERA_COXBU
ID ERA_COXBU Reviewed; 295 AA.
AC P51836;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=CBU_1502;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CB9MIC7;
RX PubMed=7830573; DOI=10.1111/j.1365-2958.1994.tb01290.x;
RA Zuber M., Hoover T.A., Powell B.S., Court D.L.;
RT "Analysis of the rnc locus of Coxiella burnetii.";
RL Mol. Microbiol. 14:291-300(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Nine Mile Crazy / RSA 514;
RX PubMed=17088354; DOI=10.1128/iai.00883-06;
RA Coleman S.A., Fischer E.R., Cockrell D.C., Voth D.E., Howe D., Mead D.J.,
RA Samuel J.E., Heinzen R.A.;
RT "Proteome and antigen profiling of Coxiella burnetii developmental forms.";
RL Infect. Immun. 75:290-298(2007).
CC -!- FUNCTION: An essential GTPase that binds both GDP and GTP, with rapid
CC nucleotide exchange. Plays a role in 16S rRNA processing and 30S
CC ribosomal subunit biogenesis and possibly also in cell cycle regulation
CC and energy metabolism. {ECO:0000255|HAMAP-Rule:MF_00367}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00367}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane
CC {ECO:0000255|HAMAP-Rule:MF_00367}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00367}.
CC -!- DEVELOPMENTAL STAGE: More than twofold more abundant in the small cell
CC variant (SCV) stage than in the large cell variant (LCV) stage (at
CC protein level). LCVs are more metabolically active than SCVs.
CC {ECO:0000269|PubMed:17088354}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00367, ECO:0000255|PROSITE-ProRule:PRU01050}.
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DR EMBL; L27436; AAA69691.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO90999.1; -; Genomic_DNA.
DR PIR; S60768; S60768.
DR RefSeq; NP_820485.1; NC_002971.3.
DR RefSeq; WP_010958267.1; NC_002971.4.
DR AlphaFoldDB; P51836; -.
DR SMR; P51836; -.
DR STRING; 227377.CBU_1502; -.
DR EnsemblBacteria; AAO90999; AAO90999; CBU_1502.
DR GeneID; 1209412; -.
DR KEGG; cbu:CBU_1502; -.
DR PATRIC; fig|227377.7.peg.1504; -.
DR eggNOG; COG1159; Bacteria.
DR HOGENOM; CLU_038009_1_2_6; -.
DR OMA; WAEVDVI; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR CDD; cd04163; Era; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00367; GTPase_Era; 1.
DR InterPro; IPR030388; G_ERA_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR005662; GTP-bd_Era.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR42698; PTHR42698; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR TIGRFAMs; TIGR00436; era; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51713; G_ERA; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Cytoplasm; GTP-binding; Membrane;
KW Nucleotide-binding; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..295
FT /note="GTPase Era"
FT /id="PRO_0000180010"
FT DOMAIN 5..172
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 203..279
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT REGION 13..20
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 39..43
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 60..63
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 121..124
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 151..153
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
SQ SEQUENCE 295 AA; 33873 MW; 559AB52D2922119E CRC64;
MKPTYCGYAA IIGRPNVGKS TLLNQLLEQK ISITSRKPQT TRYQILGVKT FKDIQVIYVD
TPGLHAGTER TINRYMNRTA RGALRDVDAI VFVIEPHWES QDAWVLDNLK EIETPVFLVI
NKVDKIKNRA ELLPLIEKVS SLYAFQKITP LSAKTGDQVG TLEQAVHQLM PESPFYFPPE
QVTDRSDQFM ASEIIREKLM RLLGQEIPYS LAVTLIEFRK EEKIIRISAV IWVEKKSQKG
IVIGKGGERL KRVGTNARLD MEKWFGKRVF LQLWVKVKSG WADNERLLRE LGFEE
